ID   K2C8_PROAT              Reviewed;         497 AA.
AC   Q5K2N3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Keratin, type II cytoskeletal 8;
DE   AltName: Full=Cytokeratin-8;
DE            Short=CK-8;
DE   AltName: Full=Keratin-8;
DE            Short=K8;
GN   Name=KRT8 {ECO:0000312|EMBL:CAH05054.1};
OS   Protopterus aethiopicus (Marbled lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Protopteridae;
OC   Protopterus.
OX   NCBI_TaxID=7886;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAH05054.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000269|PubMed:15819414};
RX   PubMed=15819414; DOI=10.1016/j.ejcb.2004.12.006;
RA   Schaffeld M., Bremer M., Hunzinger C., Markl J.;
RT   "Evolution of tissue-specific keratins as deduced from novel cDNA sequences
RT   of the lungfish Protopterus aethiopicus.";
RL   Eur. J. Cell Biol. 84:363-377(2005).
CC   -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC       to dystrophin at the costameres of striated muscle.
CC       {ECO:0000250|UniProtKB:P05787}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-8 associates with keratin-18 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC       {ECO:0000250}. Nucleus matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in skin. {ECO:0000269|PubMed:15819414}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AJ785798; CAH05054.1; -; mRNA.
DR   AlphaFoldDB; Q5K2N3; -.
DR   SMR; Q5K2N3; -.
DR   PRIDE; Q5K2N3; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Keratin; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..497
FT                   /note="Keratin, type II cytoskeletal 8"
FT                   /id="PRO_0000228677"
FT   DOMAIN          109..421
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          2..108
FT                   /note="Head"
FT   REGION          109..149
FT                   /note="Coil 1A"
FT   REGION          145..162
FT                   /note="Linker 1"
FT   REGION          163..254
FT                   /note="Coil 1B"
FT   REGION          255..278
FT                   /note="Linker 12"
FT   REGION          279..417
FT                   /note="Coil 2"
FT   REGION          418..497
FT                   /note="Tail"
FT   SITE            361
FT                   /note="Stutter"
SQ   SEQUENCE   497 AA;  55580 MW;  A660FD5EEA4C0A7A CRC64;
     MTSYQRTVTV RSSTAPKSFT SRSYTGGRFA TKASTGPLSL GSVYGGGSGR IGATTAFSTS
     TSYGGGSSFS GISAGTGFPP ITNVTVNKSL LAPLNLEIDP RIGQVRLEEK EQIKTLNNQF
     AGFIDKVRYL EQQNKLLETK WQLLQNQTTP SRSNLDSMFE AYISNLRRQL DTLGQEKGKL
     EAELHNMQGL VEDFKNKYED EINKRTDTEN EFVLIKKDVD EAYMNKVELE AKLEALTDEI
     NFLRQIYDEE IRELQTQIQD TSVIVQMDNN RQLDLDNIIA EVRAQYEDMA KKSRAEAETY
     YQQKYEELSS SAGKYGDDLR NTKNEIAELT RYINRLNSDI DALKGQRANL EAAIAEAEER
     GEQAVKNAQA QLQELQNALT QAKQDMARQL REYQELMNVK LALDIEIATY RKLLEGEESR
     LASGIQAATV QVNQSSYSGV RAPILSSGFG SGSFQTSSYS SFPLETSYSS PKKSIIVKTI
     ESRDGKIVSE RSNIVKE